Initiation of Smad-dependent and Smad-independent signaling via distinct BMP-receptor complexes.

Initiation of Smad-dependent and Smad-independent signaling via distinct BMP-receptor complexes. Research Abstract Details 

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Initiation of Smad-dependent and Smad-independent signaling via distinct BMP-receptor complexes. Abstract Text:

Sylke Hassel,Simone Schmitt,Anke Hartung,Martin Roth,Anja Nohe,Nils Petersen,Marcelo Ehrlich,Yoav I Henis,Walter Sebald,Petra Knaus,

BACKGROUND: BMP-2 (bone morphogenetic protein-2) signals via two types of transmembrane serine/threonine kinase receptors (BRI and BRII), which form heteromeric complexes prior to and after ligand binding. Within a BMP-bound receptor complex, BRII transphosphorylates and activates BRI-a for further signaling. We investigated which signaling pathway is initiated by BMP-2 via preformed receptor complexes versus BMP-2-induced signaling receptor complexes. METHODS: Immunofluorescence co-patching was used to study the oligomerization of receptors at the surface of live cells. Binding and chemical cross-linking of iodinated BMP-2 followed by immunoprecipitation was used to show association of receptors in the presence of ligand. Western blots with use of anti-phospho-Smad1 antibodies and reporter gene assays with use of SBE-lux were employed to show activation of the Smad pathway. Phosphorylation of p38-MAPK was shown by Western blots. Induction of alkaline phosphatase was determined by staining the cells. The cluster density of receptors was determined with use of image correlation spectroscopy. RESULTS AND CONCLUSION: We showed that the Smad pathway is induced by preformed receptor complexes, whereas BMP-2-induced signaling complexes result in the activation of p38-MAPK. We also found evidence that the clustering of BRI-a at the membrane is altered in the presence of BRII, suggesting that it associates with existing clusters of BRII to initiate efficient Smad signaling. These data clearly demonstrate that it is critical to fully understand receptor oligomerization in order to estimate signaling outcome for distinct receptor and ligand mutants.

Initiation of Smad-dependent and Smad-independent signaling via distinct BMP-receptor complexes. Publishing Authors By Initials

S Hassel,S Schmitt,A Hartung,M Roth,A Nohe,N Petersen,M Ehrlich,YI Henis,W Sebald,P Knaus,

For similar enzymes and coenzymes: enzymes: transferases: phosphotransferases: phosphotransferases (alcohol group acceptor): protein kinases: protein-serine-threonine kinases: mitogen-activated protein kinases: p38 mitogen-activated protein kinases research abstracts see: enzymes and coenzymes: enzymes: transferases: phosphotransferases: phosphotransferases (alcohol group acceptor): protein kinases: protein-serine-threonine kinases: mitogen-activated protein kinases: p38 mitogen-activated protein kinases research

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Initiation of Smad-dependent and Smad-independent signaling via distinct BMP-receptor complexes. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of bone and joint surgery. American vo

VOLUME: 85-A Suppl 3

Page Numbers: 44-51

Journal Abbreviation:

ISSN: 0021-9355

DAY: 19

MONTH: 11

YEAR: 2003

Initiation of Smad-dependent and Smad-independent signaling via distinct BMP-receptor complexes. Information

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LANGUAGE: eng

NlmUniqueID: 14030

Initiation of Smad-dependent and Smad-independent signaling via distinct BMP-receptor complexes. Keywords Mesh Terms:

KEYWORDS: p38 Mitogen-Activated Protein Kinases

MESH TERMS: physiology

Chemical & Substance for Abstract: Initiation of Smad-dependent and Smad-independent signaling via distinct BMP-receptor complexes. Information

Substance Name: p38 Mitogen-Activated Protein Kinases

Registry Number: EC 2.7.1.37

Grant and Affiliation Information for Initiation of Smad-dependent and Smad-independent signaling via distinct BMP-receptor complexes.

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Country: United States

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MEDLINETA: J Bone Joint Surg Am

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